ID   A0A0T0PUI6_9SPHN        Unreviewed;       964 AA.
AC   A0A0T0PUI6;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Peptidase M16 {ECO:0000313|EMBL:KQT32487.1};
GN   ORFNames=ASG29_11980 {ECO:0000313|EMBL:KQT32487.1};
OS   Sphingomonas sp. Leaf412.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1736370 {ECO:0000313|EMBL:KQT32487.1, ECO:0000313|Proteomes:UP000051178};
RN   [1] {ECO:0000313|EMBL:KQT32487.1, ECO:0000313|Proteomes:UP000051178}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf412 {ECO:0000313|EMBL:KQT32487.1,
RC   ECO:0000313|Proteomes:UP000051178};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQT32487.1, ECO:0000313|Proteomes:UP000051178}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf412 {ECO:0000313|EMBL:KQT32487.1,
RC   ECO:0000313|Proteomes:UP000051178};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KQT32487.1}.
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DR   EMBL; LMQP01000003; KQT32487.1; -; Genomic_DNA.
DR   RefSeq; WP_055984137.1; NZ_LMQP01000003.1.
DR   AlphaFoldDB; A0A0T0PUI6; -.
DR   STRING; 1736370.ASG29_11980; -.
DR   OrthoDB; 9811314at2; -.
DR   Proteomes; UP000051178; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 3.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR001431; Pept_M16_Zn_BS.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   PANTHER; PTHR43690:SF18; INSULIN-DEGRADING ENZYME-RELATED; 1.
DR   PANTHER; PTHR43690; NARDILYSIN; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 2.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 3.
DR   PROSITE; PS00143; INSULINASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051178};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          88..204
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          239..415
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          733..841
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   REGION          284..303
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   964 AA;  102913 MW;  87A2116A87FAE800 CRC64;
     MLRIPRAFAR PLAAASLLVL VADPAIGQRR APAARAAPKP VAAAPVAVDT SPWLFKGSDI
     VPDPEWYFGR LPNGLRYAVR RNGVPPGQVA VRVRIDAGSL YETDAEQGYA HLIEHLSFRG
     SKYVPDGETR RVWQRFGATF GSDSNASTTA TQTVYKLDLP GATDTKLDES LKIFAGMMSA
     PTISQVNLDS ERPAVLAEQR EAPGAQVRYG DAIRQTFFAG QPLAERSPIG TIKTLEAATP
     AAVQAFHERW YRPERTVVVI SGDLDPQVAA DLVIKNFANW RGKGPNPADP DFGTPSDAAP
     PTRTVVEPSL PPIVATAVLR PWIYRDDTII FNQKRLVDFL AVRLINRRLE TRARAGGSFL
     QASVSLDDVS RSANATFTNI VPIGDDWEAA LKDVRAVIAD AQAAPPSQAE VDRELAEFDS
     AMKNEVDTSR VEAGSKQADD MVNALDIRET VAGPRTSYDI LQEARTKGFF TPAALLESTK
     RLFTGDATRA LLNTRTADAG AAAKLAAALK ADVSGLASTR GSQAAVDFAS VPKIGKPGKV
     VARTTVGDPA MQQVTFANGV RALVHGSAAE TGRVYVRVRF GRGYQALPSD RPTVAWAGDS
     ALVPSGIGTL DQGDLDQLTT GRRIGLGFDI GDDAFVMNAQ TTPGDYADNL TLMAAKLAAP
     RWDAAPVLRA RAAMLAAYPG FRASPDAVLG GTLERSLRDG DPRWGTPALA DVQALDAKAF
     RKLWEPLLKT GPIEVQVFGD VNEDAAIDAI AKSFGALKSR RPAAIESPAV RFPAHVATPV
     MLTHDGDATQ AAAVIAWPTG GGSADHAEAR RLDVLAAIFA DRLFDRLRSA AGASYSPSAQ
     SQWPVGQAGG GRLIALGQVA PDKVDLFFRL SREIAAELVA APVGDDTLKE TVVPMLQYMA
     RASSGNQFWL LQTQGGAFDP ARIEASQNLV GDMTSITPQS LQETAAKYLR PDRDWTMAVV
     PKAK
//